ID A5K274_PLAVS Unreviewed; 493 AA. AC A5K274; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007}; DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007}; GN ORFNames=PVX_114315 {ECO:0000313|EMBL:EDL46524.1}; OS Plasmodium vivax (strain Salvador I). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=126793 {ECO:0000313|EMBL:EDL46524.1, ECO:0000313|Proteomes:UP000008333}; RN [1] {ECO:0000313|EMBL:EDL46524.1, ECO:0000313|Proteomes:UP000008333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Salvador I {ECO:0000313|EMBL:EDL46524.1, RC ECO:0000313|Proteomes:UP000008333}; RX PubMed=18843361; DOI=10.1038/nature07327; RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E., RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q., Coulson R.M., RA Crabb B.S., Del Portillo H.A., Essien K., Feldblyum T.V., RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S., RA Kooij T.W., Korsinczky M., Meyer E.V., Nene V., Paulsen I., White O., RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J., RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J., RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.; RT "Comparative genomics of the neglected human malaria parasite Plasmodium RT vivax."; RL Nature 455:757-763(2008). RN [2] {ECO:0007829|PDB:6VYF, ECO:0007829|PDB:6VYG} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), AND DISULFIDE BONDS. RX DOI=10.1107/S2052252520002456; RA Srivastava S.S., Darling J.E., Suryadi J., Morris J.C., Drew M.E., RA Subramaniam S.; RT "Plasmodium vivax and human hexokinases share similar active sites but RT display distinct quaternary architectures."; RL IUCrJ 7:453-461(2020). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+); CC Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1; CC Evidence={ECO:0000256|ARBA:ARBA00001397}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; CC Evidence={ECO:0000256|ARBA:ARBA00001397}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 1/4. CC {ECO:0000256|ARBA:ARBA00004888}. CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism. CC {ECO:0000256|ARBA:ARBA00005028}. CC -!- SIMILARITY: Belongs to the hexokinase family. CC {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EDL46524.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAKM01000003; EDL46524.1; -; Genomic_DNA. DR RefSeq; XP_001616251.1; XM_001616201.1. DR PDB; 6VYF; EM; 3.30 A; A/B/C/D=1-493. DR PDB; 6VYG; EM; 3.50 A; A/B/C/D=1-493. DR AlphaFoldDB; A5K274; -. DR EMDB; EMD-21458; -. DR EMDB; EMD-21459; -. DR SMR; A5K274; -. DR STRING; 126793.A5K274; -. DR EnsemblProtists; EDL46524; EDL46524; PVX_114315. DR GeneID; 5475550; -. DR KEGG; pvx:PVX_114315; -. DR VEuPathDB; PlasmoDB:PVX_114315; -. DR InParanoid; A5K274; -. DR OMA; ADCVQQF; -. DR PhylomeDB; A5K274; -. DR UniPathway; UPA00109; UER00180. DR Proteomes; UP000008333; Chromosome 11. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008865; F:fructokinase activity; IEA:RHEA. DR GO; GO:0005536; F:glucose binding; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 1. DR Gene3D; 3.40.367.20; -; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR001312; Hexokinase. DR InterPro; IPR019807; Hexokinase_BS. DR InterPro; IPR022673; Hexokinase_C. DR InterPro; IPR022672; Hexokinase_N. DR PANTHER; PTHR19443; HEXOKINASE; 1. DR PANTHER; PTHR19443:SF16; HEXOKINASE TYPE 1-RELATED; 1. DR Pfam; PF00349; Hexokinase_1; 1. DR Pfam; PF03727; Hexokinase_2; 1. DR PRINTS; PR00475; HEXOKINASE. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR PROSITE; PS00378; HEXOKINASE_1; 1. DR PROSITE; PS51748; HEXOKINASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:6VYF, ECO:0007829|PDB:6VYG}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU362007}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU362007}; KW Reference proteome {ECO:0000313|Proteomes:UP000008333}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}. FT DOMAIN 33..251 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 262..482 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" FT DISULFID 236..237 FT /evidence="ECO:0007829|PDB:6VYG" SQ SEQUENCE 493 AA; 55375 MW; 104B7D50068C8A4C CRC64; MSYYNLEKDD TVYYKLDTIK CDIPINEELQ ARINKHVNQL RITYSTLEEF VDNFVYELKK GLEAHRRHPN LWIPHECSFK MLDSCIADIP TGQEKGTYYA IDFGGTNFRA VRASLDGNGK IKRDQETYSL KFTGTFSHEK GLLDKHATAS QLFDHFAERI KYIMGEFKDL DNPEGKNVGF TFSFPCTSPS INCSILIDWT KGFETGRATN DPVEGRDVCK LMNDAFVRSE VPAKVCCVVN DAVGTLMSCA YQKGKTTPPC YIGIILGTGS NGCYYEPEWK KYKYSGKIIN IELGNFDKDL PLSPIDLVMD WHSANRSRQL FEKMISGAYL GEIVRRFMVN VLQSASSEKM WKSDSFNSEL GSVVLNDTSP NFEESRKVAK DAWDMDFTDE QIYALRKICE SVYNRSAALA AAAIAAIAKR IKIIEHSKFS CGVDGSLFVK NAWYCKRLQE HLKVILADKA ENLIIIPADD GSGKGAAITA AVVSQSSSIK QLP //